The N-terminal portion of an erythrotropin-like peptide from fetal bovine serum has sequence homology with the LDL-receptor and two proteins of the Epstein-Barr virus

• Published in: Biochemical and biophysical research communications Vol. 133; no. 2; pp. 404 - 409
• Main Author: Congote, L.F.
• Format: Journal Article
• Language: English
• Published: San Diego, CA Elsevier Inc 17.12.1985; Elsevier
• Subjects: Amino Acid Sequence; Animals; Applied sciences; Cattle; Chromatography, High Pressure Liquid; Epstein-Barr virus; Exact sciences and technology; Fetal Blood - analysis; Herpesvirus 4, Human; Humans; lipoprotein (low density); Liver - metabolism; N-terminus; Other techniques and industries; Peptides - blood; Receptors, LDL - analysis; Thymidine - metabolism; Viral Proteins - analysis; ELP; IGF; LDL; HPLC; TFA; ET
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1016/0006-291X(85)90920-9

An erythrotropin-like peptide (ELP) and bovine serum erythrotropin (ET) coeluted after more than four chromatographic steps. ELP was separated from ET on gel permeation high pressure liquid chromatography due to its large molecular weight. The effect of ELP on the stimulation of [ 3H]Thymidine incorporation in cell cultures of fetal bovine liver was much lower than the effect of ET. The N-terminal amino acid sequence of ELP indicated that it has a group of amino acids identical to portions of the LDL-receptor and the hypothetical proteins BHLF1 and BOLF1 deducted from the DNA sequence of the Epstein-Barr virus. These results are consistent with the idea that cell surface proteins have structural homologies with secreted proteins or some growth factor-related peptides.